ArticleThe Journal of biological chemistry2016
Structural Correlation of the Neck Coil with the Coiled-coil (CC1)-Forkhead-associated (FHA) Tandem for Active Kinesin-3 KIF13A.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The Long Haul: Microtubule Motors as the Essential Supply Line for Neuronal Longevity.Journal of neurochemistry · 2026Review
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- CCDC69 maintains genome integrity by regulating KIF2C/MCAK depolymerase activity and the stability of the chromosomal passenger complex.Scientific reports · 2024Article
- Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.BMC biology · 2022Article
- The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition.Nature communications · 2022Article
- KIF13A-A Key Regulator of Recycling Endosome Dynamics.Frontiers in cell and developmental biology · 2022Review
- KIF13A motors are regulated by Rab22A to function as weak dimers inside the cell.Science advances · 2021Article
- Coiled-coil 1-mediated fastening of the neck and motor domains for kinesin-3 autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Malleable folding of coiled-coils regulates kinesin-3 dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Intracellular Cargo Transport by Kinesin-3 Motors.Biochemistry. Biokhimiia · 2017Review
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Authors and funding
8 authors.
Funding
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Abstract
Processive kinesin motors often contain a coiled-coil neck that controls the directionality and processivity. However, the neck coil (NC) of kinesin-3 is too short to form a stable coiled-coil dimer. Here, we found that the coiled-coil (CC1)-forkhead-associated (FHA) tandem (that is connected to NC by Pro-390) of kinesin-3 KIF13A assembles as an extended dimer. With the removal of Pro-390, the NC-CC1 tandem of KIF13A unexpectedly forms a continuous coiled-coil dimer that can be well aligned into the CC1-FHA dimer. The reverse introduction of Pro-390 breaks the NC-CC1 coiled-coil dimer but provides the intrinsic flexibility to couple NC with the CC1-FHA tandem. Mutations of either NC, CC1, or the FHA domain all significantly impaired the motor activity. Thus, the three elements within the NC-CC1-FHA tandem of KIF13A are structurally interrelated to form a stable dimer for activating the motor. This work also provides the first direct structural evidence to support the formation of a coiled-coil neck by the short characteristic neck domain of kinesin-3.
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